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Structure of replicating SARS-CoV-2 polymerase.

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We determined the cryo-electron microscopy structure of the SARS-CoV-2 RNA-dependent RNA polymerase (RdRp) complex. This structure reveals how the enzyme replicates the virus genome and provides insights into antiviral drug mechanisms.

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Area of Science:

  • Structural Biology
  • Virology
  • Molecular Biology

Background:

  • Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) relies on RNA-dependent RNA polymerase (RdRp) for genome replication and gene transcription.
  • Understanding the structure of SARS-CoV-2 RdRp is crucial for developing antiviral therapies against COVID-19.

Purpose of the Study:

  • To present the cryo-electron microscopy structure of the SARS-CoV-2 RdRp in its active replicating form.
  • To elucidate the structural basis for RdRp processivity and its interaction with RNA.
  • To provide insights into the mechanisms of action for antiviral drugs targeting SARS-CoV-2 RdRp.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was employed to determine the high-resolution structure of the SARS-CoV-2 RdRp complex.
  • The structure includes viral proteins nsp12, nsp8, nsp7, and RNA template-product duplex.

Main Results:

  • The structure reveals the active-site cleft of nsp12 binding to the RNA template, mediating RdRp activity.
  • Two nsp8 molecules bind to the cleft, positioning the RNA and featuring 'sliding poles' that enhance processivity.
  • The observed structure provides a detailed molecular basis for understanding RdRp function and inhibition.

Conclusions:

  • The determined structure of the active SARS-CoV-2 RdRp complex offers a detailed molecular understanding of viral RNA replication.
  • The 'sliding poles' of nsp8 explain the enzyme's processivity, essential for replicating the long coronavirus genome.
  • This structural information facilitates the analysis of inhibitory mechanisms of antiviral drugs like remdesivir against SARS-CoV-2.